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Protein

Lysozyme C

Gene

LYZ

Organism
Pseudocheirus peregrinus (Common ring-tailed possum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiPseudocheirus peregrinus (Common ring-tailed possum)
Taxonomic identifieri9333 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDiprotodontiaPseudocheiridaePseudocheirus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›49›49Lysozyme CPRO_0000208854Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP21776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P21776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
SKMKKCEFAK IAKEQHMDGY HGVSLADWVC LVNNESDFNT KAINRNKGI
Length:49
Mass (Da):5,570
Last modified:May 1, 1991 - v1
Checksum:i8F044234322D6C2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei49 – 491

Sequence databases

PIRiPL0163.

Cross-referencesi

Sequence databases

PIRiPL0163.

3D structure databases

ProteinModelPortaliP21776.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, partial sequence and asynchronous appearance during lactation of lysozyme and alpha-lactalbumin in the milk of a marsupial, the common ringtail possum (Pseudocheirus peregrinus)."
    Nicholas K.R., Loughnan M., Messer M., Munks S., Griffiths M., Shaw D.
    Comp. Biochem. Physiol. 94B:775-778(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Milk.

Entry informationi

Entry nameiLYSC_PSEPE
AccessioniPrimary (citable) accession number: P21776
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 11, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.